Structural basis for the attachment of a paramyxoviral polymerase to its template.

@article{Kingston2004StructuralBF,
  title={Structural basis for the attachment of a paramyxoviral polymerase to its template.},
  author={Richard L. Kingston and Damon J. Hamel and L. S. Gay and Frederick W. Dahlquist and Brian W. Matthews},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2004},
  volume={101 22},
  pages={8301-6}
}
The nucleocapsid of measles virus is the template for viral RNA synthesis and is generated through packaging of the genomic RNA by the nucleocapsid protein (N). The viral polymerase associates with the nucleocapsid through a small, trihelical binding domain at the carboxyl terminus of the phosphoprotein (P). Translocation of the polymerase along the nucleocapsid during RNA synthesis is thought to involve the repeated attachment and release of the binding domain. We have investigated the… CONTINUE READING
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